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Sodium in PDB 7zsp: Human Purine Nucleoside Phosphorylase in Complex with Js-555

Enzymatic activity of Human Purine Nucleoside Phosphorylase in Complex with Js-555

All present enzymatic activity of Human Purine Nucleoside Phosphorylase in Complex with Js-555:
2.4.2.1;

Protein crystallography data

The structure of Human Purine Nucleoside Phosphorylase in Complex with Js-555, PDB code: 7zsp was solved by S.Djukic, P.Pachl, P.Rezacova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.28 / 2.29
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 142.36, 142.36, 163.61, 90, 90, 120
R / Rfree (%) 21.4 / 25.6

Other elements in 7zsp:

The structure of Human Purine Nucleoside Phosphorylase in Complex with Js-555 also contains other interesting chemical elements:

Tungsten (W) 18 atoms
Fluorine (F) 5 atoms
Tellurium (Te) 3 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Human Purine Nucleoside Phosphorylase in Complex with Js-555 (pdb code 7zsp). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Human Purine Nucleoside Phosphorylase in Complex with Js-555, PDB code: 7zsp:

Sodium binding site 1 out of 1 in 7zsp

Go back to Sodium Binding Sites List in 7zsp
Sodium binding site 1 out of 1 in the Human Purine Nucleoside Phosphorylase in Complex with Js-555


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Human Purine Nucleoside Phosphorylase in Complex with Js-555 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na305

b:88.4
occ:0.50
OE1 A:GLU8 3.3 90.9 1.0
CD A:GLU8 3.5 89.0 1.0
CG A:GLU8 3.7 84.9 1.0
CB A:GLU8 3.8 79.5 1.0
CB A:THR6 3.9 77.3 1.0
OG1 A:THR6 4.0 80.6 1.0
N A:GLU8 4.2 69.6 1.0
OE2 A:GLU8 4.2 85.2 1.0
CG2 A:THR6 4.5 80.8 1.0
N A:TYR7 4.6 62.8 1.0
CA A:GLU8 4.7 71.7 1.0
CA A:THR6 5.0 72.3 1.0

Reference:

J.Skacel, S.Djukic. Design, Synthesis, Biological Evaluation, and Crystallographic Study of Novel Pnp Inhibitors To Be Published.
Page generated: Wed Oct 9 10:19:53 2024

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